Hydrolysis of phosphohistidine in water and in prostatic acid phosphatase

Chem Commun (Camb). 2009 Nov 14:(42):6385-7. doi: 10.1039/b910451h. Epub 2009 Sep 25.

Abstract

Calculation of the free energy profile for hydrolysis of phosphohistidine using ONIOM methodology indicates a much tighter transition state in the enzyme active site compared to that in explicit water and elucidates the role of active site residues in catalysis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acid Phosphatase
  • Biocatalysis
  • Catalytic Domain
  • Histidine / analogs & derivatives*
  • Histidine / chemistry
  • Histidine / metabolism
  • Hydrolysis
  • Protein Tyrosine Phosphatases / metabolism*
  • Water / chemistry*

Substances

  • Water
  • Histidine
  • Acid Phosphatase
  • prostatic acid phosphatase
  • Protein Tyrosine Phosphatases
  • phosphohistidine